Sheep Fibrinogen gamma prime (gamma' 408-427 specific), also called Peak 2 Fibrinogen Polyclonal Antibody

Sheep anti-Fibrinogen gamma prime (Fg-gamma'), Peroxidase Conjugated IgG

Cat. Num. AAA512221

• Purity: Peroxidase conjugated IgG.; Vial containing ml of whole IgG conjugated to horseradish peroxidase (HRP) through carbohydrate groups. Total protein is 0.2 mg.
• Synonyms: Fibrinogen gamma prime (gamma' 408-427 specific); also called Peak 2 Fibrinogen; Polyclonal Antibody; Sheep anti-Fibrinogen gamma prime (Fg-gamma'); Peroxidase Conjugated IgG; human; anti-Fibrinogen gamma prime (gamma' 408-427 specific); also called Peak 2 Fibrinogen antibody

• Host: Sheep
• Clonality: Polyclonal
• Specificity: Prior to conjugation, this antibody was specific for gamma'- containing forms of fibrinogen (as demonstrated by immunoelectrophoresis and immunoblotting).
• Purity/Purification: Peroxidase conjugated IgG.; Vial containing ml of whole IgG conjugated to horseradish peroxidase (HRP) through carbohydrate groups. Total protein is 0.2 mg.
• Form/Format: IgG-HRP conjugate as a clear, slightly red-brown liquid.
• Concentration: IgG-HRP concentration is mg/ml, determined by absorbance using an extinction coefficient (E1%280) of 14. (varies by lot)

• Application Notes: Suitable as a source of peroxidase labeled antibodies to gamma'- containing forms of human fibrinogen.
• Immunogen: A synthetic peptide containing the sequence unique to the gamma' chain (VRPEHPAETEYDSLYPEDDL) conjugated to keyhole limpet hemocyanin carrier.
• Buffer: A buffered stabilizer solution containing 50% (v/v) glycerol.
• Preparation and Storage: Store between -10 and -20 degree C. Product will become viscous but will not freeze. Avoid storage in frost-free freezers. Keep vial tightly capped. Allow product to warm to room temperature and gently mix before use. Avoid exposure to sodium azide as this is an inhibitor of peroxidase activity.

Related Product Information for anti-Fibrinogen gamma prime (gamma' 408-427 specific), also called Peak 2 Fibrinogen antibody

Human fibrinogen is a 340 kDa plasma protein produced in the liver. Plasma concentrations are typically 1.7 - 3.5 g/L (5-10 uM). The intact fibrinogen molecule consists of two identical subunits, each consisting of three non-identical polypeptide chains denoted as Aalpha, Bbeta and gamma. The letters A and B in the Aalpha and Bbeta chains designate, respectively, fibrinopeptide A (FpA, residues 1-16), and fibrinopeptide B (FpB, residues 1-14), which are cleaved by thrombin upon conversion of fibrinogen to fibrin. The fibrin monomers polymerize in a half-overlap fashion to form insoluble fibrin fibrils. The polymerised fibrin is subsequently stabilized by activated Factor XIII that forms amide linkages between gamma chains and, to a lesser extent, alpha chains of the fibrin molecules. Proteolysis of fibrinogen by plasmin initially liberates C-terminal residues from the Aalpha chain to produce fragment X (intact D-E-D, which is still clottable). Fragment X is further degraded to nonclottable fragments Y (D-E) and D. Fragment Y can be digested into its constituent D and E fragments. Proteolysis of crosslinked fibrin by plasmin results in fragment DD (D-Dimer consisting of the D domains of 2 fibrin molecules crosslinked via the gamma chains), fragment E (central E domain) as well as DDE in which fragment E is noncovalently associated with DD. The molecular weights of the cleavage fragments produced from human crosslinked fibrin are: 184 kDa for fragment DD, 92 kDa for D, 50 kDa for E, 1.54 kDa for FpA and 1.57 kDa for FpB. Most of the fibrinogen in the circulation consists of 2 copies of each chain (Aalpha2, Bbeta2, gammaA2), but in normal plasma approximately 10% of the fibrinogen molecules contain one gammaA chain and one variant gamma chain (termed gamma'), in which the c-terminal AGDV residues are replaced with the amino acid sequence VRPEHPAETEYDSLYPEDDL. This variant fibrinogen is commonly referred to as fibrinogen gamma prime (gammaA/gamma') but has also been called fibrinogen 2 or peak 2 fibrinogen because it elutes separately from fibrinogen 1 (gammaA2) by ion exchange chromatography. Residues 414-427 of the gamma' chain of fibrin gamma prime (contain a high-affinity binding site for exosite II of thrombin, which allows the active site of bound thrombin to remain available to interact with substrates while demonstrating resistance to heparin mediated inhibition by antithrombin1-4.

References

1. Hantgan RR, Francis CW, Marder VJ; Fibrinogen Structure and Physiology; in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp 277-300, J.B. Lippincott Co., Philadelphia PA, USA, 1994.
2. Binnie CG, Lord ST; The Fibrinogen Sequences that Interact with Thrombin; Blood 81, pp 3186-3192, 1993.
3. Pospisil CH, Stafford AR, Fredenburgh JC, Weitz JI; Evidence that both Exosites on Thrombin Participate in Its High Affinity Interaction with Fibrin; JBC 278, pp 21584-21591, 2003.
4. Medved L, Weisel JW; Recommendations for Nomenclature on Fibrinogen and Fibrin; JTH 7, pp 355-359, 2009.